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Protein

Integrin alpha-IIb

Gene

ITGA2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi274 – 2829Sequence analysis
Calcium bindingi328 – 3369Sequence analysis
Calcium bindingi396 – 4049Sequence analysis
Calcium bindingi457 – 4659Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
SignaLinkiP08514.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-IIb
Alternative name(s):
GPalpha IIb
Short name:
GPIIb
Platelet membrane glycoprotein IIb
CD_antigen: CD41
Cleaved into the following 3 chains:
Gene namesi
Name:ITGA2B
Synonyms:GP2B, ITGAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6138. ITGA2B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 993962ExtracellularSequence analysisAdd
BLAST
Transmembranei994 – 101926HelicalSequence analysisAdd
BLAST
Topological domaini1020 – 103920CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • integrin complex Source: InterPro
  • plasma membrane Source: Reactome
  • platelet alpha granule membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Glanzmann thrombasthenia (GT)20 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
See also OMIM:273800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
VAR_030445
Natural varianti139 – 1391A → V in GT. 1 Publication
VAR_030446
Natural varianti161 – 1611C → W in GT. 1 Publication
VAR_030447
Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
VAR_030448
Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
VAR_009885
Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009886
Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
VAR_030449
Natural varianti207 – 2071T → I in GT. 1 Publication
VAR_030450
Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
Corresponds to variant rs137852911 [ dbSNP | Ensembl ].
VAR_030451
Natural varianti222 – 2221F → L in GT. 1 Publication
VAR_030452
Natural varianti267 – 2671G → E in GT. 1 Publication
VAR_030453
Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
Corresponds to variant rs137852907 [ dbSNP | Ensembl ].
VAR_003979
Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009887
Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
VAR_030454
Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
Corresponds to variant rs137852910 [ dbSNP | Ensembl ].
VAR_009888
Natural varianti358 – 3581R → H in GT; type II. 1 Publication
Corresponds to variant rs137852908 [ dbSNP | Ensembl ].
VAR_003980
Natural varianti380 – 3801G → D in GT. 1 Publication
Corresponds to variant rs766006685 [ dbSNP | Ensembl ].
VAR_030455
Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
Corresponds to variant rs75622274 [ dbSNP | Ensembl ].
VAR_030456
Natural varianti412 – 4121G → R in GT. 1 Publication
Corresponds to variant rs780786843 [ dbSNP | Ensembl ].
VAR_030457
Natural varianti449 – 4491G → D in GT; type I. 1 Publication
VAR_003981
Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
VAR_030458
Natural varianti581 – 5811A → D in GT. 1 Publication
VAR_030459
Natural varianti596 – 5961I → T in GT; type I. 3 Publications
Corresponds to variant rs76811038 [ dbSNP | Ensembl ].
VAR_030460
Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
Corresponds to variant rs77961246 [ dbSNP | Ensembl ].
VAR_030461
Natural varianti752 – 7521L → V in GT. 1 Publication
Corresponds to variant rs761174160 [ dbSNP | Ensembl ].
VAR_030462
Natural varianti755 – 7551R → P in GT. 1 Publication
Corresponds to variant rs763762304 [ dbSNP | Ensembl ].
VAR_030463
Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
Corresponds to variant rs74475415 [ dbSNP | Ensembl ].
VAR_003982
Natural varianti847 – 8471L → P in GT. 1 Publication
VAR_030464
Natural varianti934 – 9341V → F in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 Publication
VAR_069917
Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
VAR_030465
Natural varianti957 – 9571S → L in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein. 1 Publication
Corresponds to variant rs80002943 [ dbSNP | Ensembl ].
VAR_069918
Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
Corresponds to variant rs78657866 [ dbSNP | Ensembl ].
VAR_030466
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Bleeding disorder, platelet-type 16 (BDPLT16)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities.
See also OMIM:187800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
VAR_069919

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1029 – 10302PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiITGA2B.
MIMi187800. phenotype.
273800. phenotype.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA29938.

Chemistry

ChEMBLiCHEMBL2093869.
DrugBankiDB00054. Abciximab.
DB00775. Tirofiban.

Polymorphism and mutation databases

BioMutaiITGA2B.
DMDMi226694183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31313 PublicationsAdd
BLAST
Chaini32 – 10391008Integrin alpha-IIbPRO_0000016275Add
BLAST
Chaini32 – 887856Integrin alpha-IIb heavy chainPRO_0000016276Add
BLAST
Chaini891 – 1039149Integrin alpha-IIb light chain, form 1PRO_0000292348Add
BLAST
Chaini903 – 1039137Integrin alpha-IIb light chain, form 2PRO_0000016277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 961 Publication
Disulfide bondi138 ↔ 1611 Publication
Disulfide bondi177 ↔ 1981 Publication
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
Disulfide bondi504 ↔ 5151 Publication
Disulfide bondi521 ↔ 5761 Publication
Glycosylationi601 – 6011N-linked (GlcNAc...)2 Publications
Disulfide bondi633 ↔ 6391 Publication
Disulfide bondi705 ↔ 7181 Publication
Glycosylationi711 – 7111N-linked (GlcNAc...)1 Publication
Disulfide bondi857 ↔ 911Interchain (between heavy and light chains)1 Publication
Glycosylationi874 – 8741O-linked (GalNAc...); in alloantigen HPA-3B
Glycosylationi878 – 8781O-linked (GalNAc...)1 Publication
Modified residuei891 – 8911Pyrrolidone carboxylic acid; in light chain form 11 Publication
Disulfide bondi916 ↔ 9211 Publication
Glycosylationi962 – 9621N-linked (GlcNAc...)

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP08514.
PeptideAtlasiP08514.
PRIDEiP08514.
TopDownProteomicsiP08514-1. [P08514-1]

2D gel databases

OGPiP08514.

PTM databases

iPTMnetiP08514.
PhosphoSiteiP08514.

Miscellaneous databases

PMAP-CutDBQ17R67.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

Gene expression databases

BgeeiENSG00000005961.
CleanExiHS_ITGA2B.
ExpressionAtlasiP08514. baseline and differential.
GenevisibleiP08514. HS.

Organism-specific databases

HPAiCAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-702693,EBI-702693
ITGB3P0510611EBI-702693,EBI-702847

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi109881. 11 interactions.
DIPiDIP-68N.
IntActiP08514. 2 interactions.
STRINGi9606.ENSP00000262407.

Chemistry

BindingDBiP08514.

Structurei

Secondary structure

1
1039
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Beta strandi40 – 434Combined sources
Beta strandi52 – 587Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 707Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 887Combined sources
Beta strandi93 – 953Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi160 – 1645Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 1744Combined sources
Helixi183 – 1886Combined sources
Turni189 – 1935Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi211 – 2166Combined sources
Helixi219 – 2224Combined sources
Beta strandi225 – 2306Combined sources
Helixi231 – 2377Combined sources
Helixi259 – 2613Combined sources
Beta strandi268 – 2736Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi283 – 2886Combined sources
Helixi291 – 2944Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi336 – 3416Combined sources
Beta strandi345 – 3484Combined sources
Turni349 – 3513Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi375 – 3795Combined sources
Beta strandi391 – 3955Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi404 – 4096Combined sources
Beta strandi413 – 4175Combined sources
Beta strandi419 – 4235Combined sources
Beta strandi427 – 4304Combined sources
Beta strandi435 – 4395Combined sources
Beta strandi450 – 4567Combined sources
Beta strandi458 – 4636Combined sources
Beta strandi465 – 4706Combined sources
Helixi471 – 4733Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi484 – 49310Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi512 – 52514Combined sources
Beta strandi534 – 5418Combined sources
Turni542 – 5443Combined sources
Helixi547 – 5493Combined sources
Beta strandi551 – 5544Combined sources
Turni555 – 5573Combined sources
Beta strandi559 – 5679Combined sources
Beta strandi575 – 5839Combined sources
Helixi586 – 5883Combined sources
Beta strandi596 – 6038Combined sources
Beta strandi616 – 6194Combined sources
Beta strandi622 – 6276Combined sources
Turni634 – 6374Combined sources
Beta strandi643 – 6519Combined sources
Beta strandi653 – 6553Combined sources
Beta strandi662 – 6709Combined sources
Beta strandi678 – 6836Combined sources
Beta strandi688 – 6958Combined sources
Beta strandi705 – 7084Combined sources
Beta strandi710 – 7134Combined sources
Beta strandi715 – 7217Combined sources
Beta strandi728 – 73811Combined sources
Beta strandi746 – 75510Combined sources
Beta strandi759 – 7613Combined sources
Beta strandi767 – 7748Combined sources
Beta strandi779 – 79214Combined sources
Beta strandi810 – 81910Combined sources
Beta strandi821 – 8233Combined sources
Beta strandi825 – 83612Combined sources
Beta strandi842 – 85413Combined sources
Beta strandi856 – 8616Combined sources
Beta strandi906 – 9094Combined sources
Turni911 – 9133Combined sources
Beta strandi916 – 92611Combined sources
Beta strandi931 – 94010Combined sources
Helixi942 – 9454Combined sources
Beta strandi952 – 96514Combined sources
Beta strandi967 – 9693Combined sources
Beta strandi977 – 98812Combined sources
Turni991 – 9944Combined sources
Helixi997 – 102024Combined sources
Beta strandi1022 – 10243Combined sources
Turni1025 – 10273Combined sources
Helixi1028 – 10314Combined sources
Turni1035 – 10384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2MTPNMR-B1019-1039[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
4Z7NX-ray2.60A/C32-486[»]
4Z7OX-ray2.85A/C32-486[»]
4Z7QX-ray2.70A/C32-485[»]
5HDBX-ray2.70A/C32-485[»]
ProteinModelPortaliP08514.
SMRiP08514. Positions 32-989, 991-1039.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 9662FG-GAP 1PROSITE-ProRule annotationAdd
BLAST
Repeati110 – 17364FG-GAP 2PROSITE-ProRule annotationAdd
BLAST
Repeati187 – 23852FG-GAP 3PROSITE-ProRule annotationAdd
BLAST
Repeati251 – 30555FG-GAP 4PROSITE-ProRule annotationAdd
BLAST
Repeati306 – 37166FG-GAP 5PROSITE-ProRule annotationAdd
BLAST
Repeati373 – 43260FG-GAP 6PROSITE-ProRule annotationAdd
BLAST
Repeati435 – 49662FG-GAP 7PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1022 – 10265GFFKR motif

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08514.
KOiK06476.
OMAiLWLLEWV.
OrthoDBiEOG091G05Z4.
PhylomeDBiP08514.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08514-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF
60 70 80 90 100
GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL
110 120 130 140 150
FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT
160 170 180 190 200
EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA
210 220 230 240 250
GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ
260 270 280 290 300
SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI
310 320 330 340 350
LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD
360 370 380 390 400
RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD
410 420 430 440 450
GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF
460 470 480 490 500
SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA
510 520 530 540 550
VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR
560 570 580 590 600
RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL
610 620 630 640 650
NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT
660 670 680 690 700
GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF
710 720 730 740 750
ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF
760 770 780 790 800
QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE
810 820 830 840 850
QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ
860 870 880 890 900
PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP
910 920 930 940 950
SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL
960 970 980 990 1000
DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV
1010 1020 1030
LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE
Length:1,039
Mass (Da):113,377
Last modified:April 14, 2009 - v3
Checksum:i063EE298E026F116
GO
Isoform 2 (identifier: P08514-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     948-981: Missing.

Show »
Length:1,005
Mass (Da):109,574
Checksum:i81C09F0D904CB534
GO
Isoform 3 (identifier: P08514-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

Show »
Length:953
Mass (Da):103,218
Checksum:i0100D4C5919320BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231P → A in AAA35926 (PubMed:2345548).Curated
Sequence conflicti120 – 1201A → S in BAG37735 (PubMed:14702039).Curated
Sequence conflicti287 – 2882GA → VP in AAA53150 (PubMed:2322558).Curated
Sequence conflicti346 – 3461E → D in AAA35926 (PubMed:2345548).Curated
Sequence conflicti565 – 5651N → D in AAA35926 (PubMed:2345548).Curated
Sequence conflicti566 – 5661L → V in CAA29987 (PubMed:3422188).Curated
Sequence conflicti633 – 6331C → S in AAA60114 (PubMed:2439501).Curated
Sequence conflicti729 – 7291Q → E in CAA29987 (PubMed:3422188).Curated
Sequence conflicti971 – 9711P → A in AAA53150 (PubMed:2322558).Curated
Sequence conflicti1029 – 10291P → H in AAA35926 (PubMed:2345548).Curated
Sequence conflicti1029 – 10291P → H in AAA52588 (PubMed:2845986).Curated
Sequence conflicti1030 – 10301P → T in AAA52588 (PubMed:2845986).Curated

Polymorphismi

Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401T → I.1 Publication
Corresponds to variant rs5915 [ dbSNP | Ensembl ].
VAR_014176
Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
VAR_030445
Natural varianti139 – 1391A → V in GT. 1 Publication
VAR_030446
Natural varianti161 – 1611C → W in GT. 1 Publication
VAR_030447
Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
VAR_030448
Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
VAR_009885
Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009886
Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
VAR_030449
Natural varianti207 – 2071T → I in GT. 1 Publication
VAR_030450
Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
Corresponds to variant rs137852911 [ dbSNP | Ensembl ].
VAR_030451
Natural varianti222 – 2221F → L in GT. 1 Publication
VAR_030452
Natural varianti267 – 2671G → E in GT. 1 Publication
VAR_030453
Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
Corresponds to variant rs137852907 [ dbSNP | Ensembl ].
VAR_003979
Natural varianti313 – 3131G → A.2 Publications
Corresponds to variant rs1126554 [ dbSNP | Ensembl ].
VAR_054820
Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009887
Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
VAR_030454
Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
Corresponds to variant rs137852910 [ dbSNP | Ensembl ].
VAR_009888
Natural varianti358 – 3581R → H in GT; type II. 1 Publication
Corresponds to variant rs137852908 [ dbSNP | Ensembl ].
VAR_003980
Natural varianti380 – 3801G → D in GT. 1 Publication
Corresponds to variant rs766006685 [ dbSNP | Ensembl ].
VAR_030455
Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
Corresponds to variant rs75622274 [ dbSNP | Ensembl ].
VAR_030456
Natural varianti412 – 4121G → R in GT. 1 Publication
Corresponds to variant rs780786843 [ dbSNP | Ensembl ].
VAR_030457
Natural varianti449 – 4491G → D in GT; type I. 1 Publication
VAR_003981
Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
VAR_030458
Natural varianti581 – 5811A → D in GT. 1 Publication
VAR_030459
Natural varianti596 – 5961I → T in GT; type I. 3 Publications
Corresponds to variant rs76811038 [ dbSNP | Ensembl ].
VAR_030460
Natural varianti649 – 6491V → L.
Corresponds to variant rs7207402 [ dbSNP | Ensembl ].
VAR_054821
Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
Corresponds to variant rs77961246 [ dbSNP | Ensembl ].
VAR_030461
Natural varianti752 – 7521L → V in GT. 1 Publication
Corresponds to variant rs761174160 [ dbSNP | Ensembl ].
VAR_030462
Natural varianti755 – 7551R → P in GT. 1 Publication
Corresponds to variant rs763762304 [ dbSNP | Ensembl ].
VAR_030463
Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
Corresponds to variant rs74475415 [ dbSNP | Ensembl ].
VAR_003982
Natural varianti847 – 8471L → P in GT. 1 Publication
VAR_030464
Natural varianti874 – 8741I → S Alloantigen HPA-3B. 1 Publication
Corresponds to variant rs5911 [ dbSNP | Ensembl ].
VAR_003983
Natural varianti934 – 9341V → F in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 Publication
VAR_069917
Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
VAR_030465
Natural varianti957 – 9571S → L in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein. 1 Publication
Corresponds to variant rs80002943 [ dbSNP | Ensembl ].
VAR_069918
Natural varianti968 – 9681Y → N.1 Publication
Corresponds to variant rs5914 [ dbSNP | Ensembl ].
VAR_014177
Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
Corresponds to variant rs78657866 [ dbSNP | Ensembl ].
VAR_030466
Natural varianti989 – 9891A → T.2 Publications
Corresponds to variant rs78165611 [ dbSNP | Ensembl ].
VAR_030467
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
VAR_069919

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei910 – 1039130SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3. CuratedVSP_002736Add
BLAST
Alternative sequencei948 – 98134Missing in isoform 2. CuratedVSP_002737Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSiCCDS32665.1. [P08514-1]
PIRiA34269.
RefSeqiNP_000410.2. NM_000419.4. [P08514-1]
XP_011523051.1. XM_011524749.1. [P08514-2]
UniGeneiHs.411312.

Genome annotation databases

EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
GeneIDi3674.
KEGGihsa:3674.
UCSCiuc002igt.2. human. [P08514-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSiCCDS32665.1. [P08514-1]
PIRiA34269.
RefSeqiNP_000410.2. NM_000419.4. [P08514-1]
XP_011523051.1. XM_011524749.1. [P08514-2]
UniGeneiHs.411312.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2MTPNMR-B1019-1039[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
4Z7NX-ray2.60A/C32-486[»]
4Z7OX-ray2.85A/C32-486[»]
4Z7QX-ray2.70A/C32-485[»]
5HDBX-ray2.70A/C32-485[»]
ProteinModelPortaliP08514.
SMRiP08514. Positions 32-989, 991-1039.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109881. 11 interactions.
DIPiDIP-68N.
IntActiP08514. 2 interactions.
STRINGi9606.ENSP00000262407.

Chemistry

BindingDBiP08514.
ChEMBLiCHEMBL2093869.
DrugBankiDB00054. Abciximab.
DB00775. Tirofiban.

PTM databases

iPTMnetiP08514.
PhosphoSiteiP08514.

Polymorphism and mutation databases

BioMutaiITGA2B.
DMDMi226694183.

2D gel databases

OGPiP08514.

Proteomic databases

PaxDbiP08514.
PeptideAtlasiP08514.
PRIDEiP08514.
TopDownProteomicsiP08514-1. [P08514-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
GeneIDi3674.
KEGGihsa:3674.
UCSCiuc002igt.2. human. [P08514-1]

Organism-specific databases

CTDi3674.
GeneCardsiITGA2B.
HGNCiHGNC:6138. ITGA2B.
HPAiCAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.
MalaCardsiITGA2B.
MIMi187800. phenotype.
273800. phenotype.
607759. gene.
neXtProtiNX_P08514.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA29938.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08514.
KOiK06476.
OMAiLWLLEWV.
OrthoDBiEOG091G05Z4.
PhylomeDBiP08514.
TreeFamiTF105391.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
SignaLinkiP08514.

Miscellaneous databases

ChiTaRSiITGA2B. human.
EvolutionaryTraceiP08514.
GeneWikiiITGA2B.
GenomeRNAii3674.
PMAP-CutDBQ17R67.
PROiP08514.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005961.
CleanExiHS_ITGA2B.
ExpressionAtlasiP08514. baseline and differential.
GenevisibleiP08514. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITA2B_HUMAN
AccessioniPrimary (citable) accession number: P08514
Secondary accession number(s): B2RCY8
, O95366, Q14443, Q17R67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 14, 2009
Last modified: September 7, 2016
This is version 209 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.